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Vol. 273, Issue 4, 2336-2343, January 23, 1998

Protein Kinase C-dependent Tyrosine Phosphorylation of p130^cas in Differentiating Neuroblastoma Cells

From the Department of Laboratory Medicine, Lund University, University Hospital MAS, S-205 02 Malmö and the ^§ Department of Pathology, University Hospital, S-751 85 Uppsala, Sweden

The cell signaling docking protein p130^cas became tyrosine-phosphorylated in SH-SY5Y human neuroblastoma cells during induced differentiation with 12-O-tetradecanoylphorbol-13-acetate (TPA) and serum or a combination of basic fibroblast growth factor (bFGF) and insulin-like growth factor-I (IGF-I). The differentiating cells develop a neuronal phenotype with neurites and growth cones and sustained activation of protein kinase C (PKC) and pp60^c-src. The TPA-induced p130^cas phosphorylation increased within 5 min of stimulation and persisted for at least 4 days, whereas bFGF/IGF-I-induced p130^cas phosphorylation was biphasic. However, the increase in tyrosine phosphorylation of p130^cas was not restricted to differentiation inducing stimuli. The phosphorylation was blocked by the specific PKC inhibitor GF 109203X, and transient transfection with active PKC- induced p130^cas tyrosine phosphorylation. pp60^c-src, known to directly phosphorylate p130^cas in other cell systems, was not activated after stimulation with TPA or bFGF/IGF-I for up to 30 min, and the initial p130^cas phosphorylation was resistant to the Src family kinase inhibitor herbimycin A. However, in long term stimulated cells, herbimycin A blocked the induced phosphorylation of p130^cas. Also, overexpression of src induced phosphorylation of p130^cas. p130^cas protein and phosphorylated p130^cas were present in growth cones isolated from differentiated SH-SY5Y cells. Inhibition of PKC activity in differentiating cells with GF 109203X leads to a rapid retraction of growth cone filopodia, and p130^cas phosphorylation decreased transiently (within minutes). Growth cones isolated from these cells were virtually devoid of phosphorylated p130^cas. These data suggest a function for p130^cas as a PKC downstream target in SH-SY5Y cells and possibly also in their growth cones.

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